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Journal articles on the topic 'Amyloid beta (1-40)'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Zheng, Weihua, Min-Yeh Tsai, and Peter G. Wolynes. "Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1–42) and Amyloid Beta(1–40)." Journal of the American Chemical Society 139, no. 46 (November 7, 2017): 16666–76. http://dx.doi.org/10.1021/jacs.7b08089.

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2

Chrambach, Adam, Andreas Chrambach, and Sheryl K. Brining. "Gel electrophoretic distinction between Congo Red nonreactive beta-amyloid (1—42) and beta-amyloid (1—40)." Electrophoresis 21, no. 4 (March 1, 2000): 760–61. http://dx.doi.org/10.1002/(sici)1522-2683(20000301)21:4<760::aid-elps760>3.0.co;2-5.

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3

Usui, Kenji, Shin-ichiro Yokota, Kazuya Iwata, and Yoshio Hamada. "Novel Purification Process for Amyloid Beta Peptide(1-40)." Processes 8, no. 4 (April 15, 2020): 464. http://dx.doi.org/10.3390/pr8040464.

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Amyloid beta peptide (Aβ)-related studies require an adequate supply of purified Aβ peptide. However, Aβ peptides are “difficult sequences” to synthesize chemically, and low yields are common due to aggregation during purification. Here, we demonstrate an easier synthesis, deprotection, reduction, cleavage, and purification process for Aβ(1-40) using standard 9-fluorenylmethyloxycarbonyl (Fmoc)-protected amino acids and solid-phase peptide synthesis (SPPS) resin [HMBA (4-hydroxymethyl benzamide) resin] that provides higher yields of Aβ(1-40) than previous standard protocols. Furthermore, purification requires a similar amount of time as conventional purification processes, although the peptide must be cleaved from the resin immediately prior to purification. The method described herein is not limited to the production of Aβ(1-40), and can be used to synthesize other easily-oxidized and aggregating sequences. Our proposed methodology will contribute to various fields using “difficult sequence” peptides, such as pharmaceutical and materials science, as well as research for the diagnosis and treatment of protein/peptide misfolding diseases.

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4

Belitzky, Alik, Naomi Melamed-Book, Aryeh Weiss, and Uri Raviv. "The dynamic nature of amyloid beta (1–40) aggregation." Physical Chemistry Chemical Physics 13, no. 30 (2011): 13809. http://dx.doi.org/10.1039/c1cp20832b.

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5

Stamatelopoulos, Kimon, Christine J. Pol, Colby Ayers, Georgios Georgiopoulos, Aikaterini Gatsiou, Emmanouil S. Brilakis, Amit Khera, Konstantinos Drosatos, James A. de Lemos, and Konstantinos Stellos. "Amyloid-Beta (1-40) Peptide and Subclinical Cardiovascular Disease." Journal of the American College of Cardiology 72, no. 9 (August 2018): 1060–61. http://dx.doi.org/10.1016/j.jacc.2018.06.027.

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6

Cleary, James, Jodie M. Hittner, Michael Semotuk, Patrick Mantyh, and Eugene O'Hare. "Beta-amyloid(1–40) effects on behavior and memory." Brain Research 682, no. 1-2 (June 1995): 69–74. http://dx.doi.org/10.1016/0006-8993(95)00323-i.

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7

Pérez, Virginia, Noelia Fandos, Pedro Pesini, and Manuel Sarasa. "P1-244: Validation of beta-amyloid test as a reliable tool for quantifying beta-amyloid 1-40 and beta-amyloid 1-42 in blood." Alzheimer's & Dementia 9 (July 2013): P241. http://dx.doi.org/10.1016/j.jalz.2013.05.468.

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8

Cerofolini, Linda, Enrico Ravera, Sara Bologna, Thomas Wiglenda, Annett Böddrich, Bettina Purfürst, Iryna Benilova, et al. "Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils." Chemical Communications 56, no. 62 (2020): 8830–33. http://dx.doi.org/10.1039/d0cc02463e.

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9

KLEIN, AUTUMN M., NEIL W. KOWALL, and ROBERT J. FERRANTE. "Neurotoxicity and Oxidative Damage of Beta Amyloid 1-42 versus Beta Amyloid 1-40 in the Mouse Cerebral Cortex." Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (November 1999): 314–20. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07845.x.

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10

Maltseva, Elena, and Gerald Brezesinski. "Adsorption of Amyloid Beta (1-40) Peptide to Phosphatidylethanolamine Monolayers." ChemPhysChem 5, no. 8 (August 20, 2004): 1185–90. http://dx.doi.org/10.1002/cphc.200400045.

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11

Atchison, Kevin, Claude Ambroise, Christine Oborski, Leslie Pustilnik, Stephen Noell, Michael Brodney, ONeill Brian, Charles Nolan, and David Riddell. "P1-109: Inhibition of BACE1 reduces beta-amyloid 1-40 but not N-terminal-truncated beta-amyloid." Alzheimer's & Dementia 9 (July 2013): P190. http://dx.doi.org/10.1016/j.jalz.2013.05.331.

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12

Caba, Ioana Cezara, Raluca Ştefănescu, and Bogdan Ionel Tamba. "Observation of Intact and Proteolytically Cleaved Amyloid-Beta (1–40)-Oleuropein Noncovalent Complex at Neutral pH by Mass Spectrometry." Molecules 26, no. 11 (May 28, 2021): 3261. http://dx.doi.org/10.3390/molecules26113261.

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Mass spectrometry analyses carried out on mass spectrometers equipped with soft ionization sources demonstrated their utility in the assessment of the formation of noncovalent complexes and the localization of the binding sites. Direct analyses by mass spectrometry of the noncovalent complex formed in acidic and mildly acidic environments by amyloid beta (1–40) peptide and oleuropein have been previously described, and, in several studies, the absorption, metabolism, excretion, and the implications in the prevention and therapy of Alzheimer’s disease of oleuropein have been investigated. Our paper presents modifications of the method previously employed for noncovalent complex observation, namely, the amyloid beta (1–40) pretreatment, followed by an increase in the pH and replacement of the chemical environment from ammonium acetate to ammonium bicarbonate. The formation of noncovalent complexes with one or two molecules of oleuropein was detected in all chemical solutions used, and the amyloid beta (17–28) binding site was identified via proteolytic experiments using trypsin prior to and after noncovalent complex formation. Our results highlight the importance of further studies on the effect of oleuropein against amyloid beta aggregation.

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13

Gaskin, F., J. Finley, Q. Fang, S. Xu, and S. M. Fu. "Human antibodies reactive with beta-amyloid protein in Alzheimer's disease." Journal of Experimental Medicine 177, no. 4 (April 1, 1993): 1181–86. http://dx.doi.org/10.1084/jem.177.4.1181.

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Four human B cell lines established by Epstein-Barr viral transformation of B cells from a patient with a clinical diagnosis of Alzheimer's disease (AD) were found to secrete antibodies that react with plaques and cerebrovascular blood vessels in AD brain in a staining profile characteristic of beta-amyloid protein (beta-AP) in AD brain. Two of these antibodies were shown to be reactive with a rare plaque in a normal brain. In these studies, immunofluorescence and avidin-biotin complex immunoperoxidase methodology were used to determine antibody reaction, and thioflavine S was used to double label amyloid and neurofibrillary tangles. The four antibodies also reacted with neurons in normal and AD brain. Absorption studies, dot immunoblots, and enzyme-linked immunosorbent assays with beta-amyloid peptides 1-28 (beta-A1-28) and 1-40 (beta-A1-40) indicate the major determinant of the reactive epitope is located in the region of amino acids 1-28 of beta-AP. However, inhibition studies demonstrate a significant contribution to the antigenic determinant by the 29-40 region of the beta-A1-40. These antibodies represent the first human autoantibodies against beta-AP. The pathological significance of these autoantibodies is discussed.

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14

Brining, Sheryl K. "Predicting the In Vitro Toxicity of Synthetic Beta-Amyloid (1-40)." Neurobiology of Aging 18, no. 6 (November 1997): 581–89. http://dx.doi.org/10.1016/s0197-4580(97)00153-x.

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15

Kulstad, J. Jacob, Christopher E. Savard, Sum P. Lee, Suzanne Craft, and David G. Cook. "P2-020: Liver-mediated clearance of peripheral amyloid-beta (1-40)." Alzheimer's & Dementia 2 (July 2006): S237—S238. http://dx.doi.org/10.1016/j.jalz.2006.05.857.

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16

Foschi, Giulia, Cristiano Albonetti, Fabiola Liscio, Silvia Milita, Pierpaolo Greco, and Fabio Biscarini. "Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space." ChemPhysChem 16, no. 16 (September 14, 2015): 3379–84. http://dx.doi.org/10.1002/cphc.201500602.

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17

Rasoolijazi, H., N. Azad, M. T. Joghataei, M. Kerdari, F. Nikbakht, and M. Soleimani. "The Protective Role of Carnosic Acid against Beta-Amyloid Toxicity in Rats." Scientific World Journal 2013 (2013): 1–5. http://dx.doi.org/10.1155/2013/917082.

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Oxidative stress is one of the pathological mechanisms responsible for the beta- amyloid cascade associated with Alzheimer’s disease (AD). Previous studies have demonstrated the role of carnosic acid (CA), an effective antioxidant, in combating oxidative stress. A progressive cognitive decline is one of the hallmarks of AD. Thus, we attempted to determine whether the administration of CA protects against memory deficit caused by beta-amyloid toxicity in rats. Beta-amyloid (1–40) was injected by stereotaxic surgery into the Ca1 region of the hippocampus of rats in the Amyloid beta (Aβ) groups. CA was delivered intraperitoneally, before and after surgery in animals in the CA groups. Passive avoidance learning and spontaneous alternation behavior were evaluated using the shuttle box and the Y-maze, respectively. The degenerating hippocampal neurons were detected by fluoro-jade b staining. We observed that beta-amyloid (1–40) can induce neurodegeneration in the Ca1 region of the hippocampus by using fluoro-jade b staining. Also, the behavioral tests revealed that CA may recover the passive avoidance learning and spontaneous alternation behavior scores in the Aβ+ CA group, in comparison with the Aβgroup. We found that CA may ameliorate the spatial and learning memory deficits induced by the toxicity of beta-amyloid in the rat hippocampus.

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18

Bayes-Genis, Antoni, Jaume Barallat, Marta de Antonio, Mar Domingo, Elisabet Zamora, Joan Vila, Isaac Subirana, et al. "Bloodstream Amyloid-beta (1-40) Peptide, Cognition, and Outcomes in Heart Failure." Revista Española de Cardiología (English Edition) 70, no. 11 (November 2017): 924–32. http://dx.doi.org/10.1016/j.rec.2017.02.021.

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19

Pijnenburg, Y. A. L., S. N. M. Schoonenboom, P. D. Mehta, S. P. Mehta, C. Mulder, R. Veerhuis, M. A. Blankenstein, and P. Scheltens. "Decreased cerebrospinal fluid amyloid beta (1-40) levels in frontotemporal lobar degeneration." Journal of Neurology, Neurosurgery & Psychiatry 78, no. 7 (December 18, 2006): 735–37. http://dx.doi.org/10.1136/jnnp.2006.105064.

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20

Jiang, H., D. Burdick, C. G. Glabe, C. W. Cotman, and A. J. Tenner. "beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain." Journal of Immunology 152, no. 10 (May 15, 1994): 5050–59. http://dx.doi.org/10.4049/jimmunol.152.10.5050.

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Abstract beta-amyloid peptides that accumulate within the brain of individuals with Alzheimer's disease bind to C1q and activate the classical C pathway via a specific interaction with a site within the collagen-like domain of C1q (C1q-CLF). Synthetic analogues of beta-amyloid peptides, beta 1-42 and beta 1-40, bound to C1q and were strong activators of C as assessed by both total C consumption and C4 consumption. beta 1-42 was significantly more effective than beta 1-40 in binding to C1q and triggering C activation, whereas beta 1-28 demonstrated little or no binding or C activation. This C-activating capacity seems to be largely correlated with the assembly of the beta 1-42 into low speed sedimentable aggregates and/or macromolecular fibrils. Radiolabeled C1q and C1q-CLF bind specifically to these aggregates or amyloid fibrils. In addition, using synthetic C1q peptides in a solid phase binding assay, the major binding site of beta 1-42 to C1q was localized to the C1q A chain collagen-like residues 14-26, a region previously described as a novel interaction site for Ab-independent activators of C1. C1q A chain peptide 14-26 blocked the ability of beta-amyloid peptides to activate the classical C pathway, providing evidence that this relatively unrecognized mechanism of C activation (via binding to the C1q-CLF) may have crucial physiologic consequences. Finally, these observations provide further support for the hypothesis that C activation and inflammation may be a component in the pathogenesis of AD and suggest possibilities for modulating the progression of AD.

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21

Morel, Bertrand, María P. Carrasco-Jiménez, Samuel Jurado, and Francisco Conejero-Lara. "Rapid Conversion of Amyloid-Beta 1-40 Oligomers to Mature Fibrils through a Self-Catalytic Bimolecular Process." International Journal of Molecular Sciences 22, no. 12 (June 14, 2021): 6370. http://dx.doi.org/10.3390/ijms22126370.

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The formation of fibrillar aggregates of the amyloid beta peptide (Aβ) in the brain is one of the hallmarks of Alzheimer’s disease (AD). A clear understanding of the different aggregation steps leading to fibrils formation is a keystone in therapeutics discovery. In a recent study, we showed that Aβ40 and Aβ42 form dynamic micellar aggregates above certain critical concentrations, which mediate a fast formation of more stable oligomers, which in the case of Aβ40 are able to evolve towards amyloid fibrils. Here, using different biophysical techniques we investigated the role of different fractions of the Aβ aggregation mixture in the nucleation and fibrillation steps. We show that both processes occur through bimolecular interplay between low molecular weight species (monomer and/or dimer) and larger oligomers. Moreover, we report here a novel self-catalytic mechanism of fibrillation of Aβ40, in which early oligomers generate and deliver low molecular weight amyloid nuclei, which then catalyze the rapid conversion of the oligomers to mature amyloid fibrils. This fibrillation catalytic activity is not present in freshly disaggregated low-molecular weight Aβ40 and is, therefore, a property acquired during the aggregation process. In contrast to Aβ40, we did not observe the same self-catalytic fibrillation in Aβ42 spheroidal oligomers, which could neither be induced to fibrillate by the Aβ40 nuclei. Our results reveal clearly that amyloid fibrillation is a multi-component process, in which dynamic collisions between different interacting species favor the kinetics of amyloid nucleation and growth.

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22

Saito, Y., J. Buciak, J. Yang, and W. M. Pardridge. "Vector-mediated delivery of 125I-labeled beta-amyloid peptide A beta 1-40 through the blood-brain barrier and binding to Alzheimer disease amyloid of the A beta 1-40/vector complex." Proceedings of the National Academy of Sciences 92, no. 22 (October 24, 1995): 10227–31. http://dx.doi.org/10.1073/pnas.92.22.10227.

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23

Sahoo, Bikash R., Takuya Genjo, Michael Bekier, Sarah J. Cox, Andrea K. Stoddard, Magdalena Ivanova, Kazuma Yasuhara, Carol A. Fierke, Yanzhuang Wang, and Ayyalusamy Ramamoorthy. "Alzheimer's amyloid-beta intermediates generated using polymer-nanodiscs." Chemical Communications 54, no. 91 (2018): 12883–86. http://dx.doi.org/10.1039/c8cc07921h.

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24

Robshaw, Ashley, Kevin Atchison, Claude Ambroise, Charles Nolan, Kathleen Wood, Cathleen Gonzales, Christine Oborski, Feng Pan, Eva Hajos-Korcsok, and David Riddell. "P2-394: Characterization of beta-amyloid 1-40 across species following treatment with beta-secretase inhibitors." Alzheimer's & Dementia 9 (July 2013): P502. http://dx.doi.org/10.1016/j.jalz.2013.05.1043.

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25

Liu, Sijun, Yuying Zhao, Xiaoying Su, Chengcheng Zhou, Peifen Yang, Qiusan Lin, Shijun Li, et al. "Reconstruction of Alzheimer’s Disease Cell Model In Vitro via Extracted Peripheral Blood Molecular Cells from a Sporadic Patient." Stem Cells International 2020 (December 18, 2020): 1–10. http://dx.doi.org/10.1155/2020/8897494.

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The establishment of human-induced pluripotent stem cell (iPSC) models from sporadic Alzheimer’s disease (sAD) patients is necessary and could potentially benefit research into disease etiology and therapeutic strategies. However, the development of sAD iPSC models is still limited due to the multifactorial nature of the disease. Here, we extracted peripheral blood mononuclear cells (PBMCs) from a patient with sAD and induced them into iPSC by introducing the Sendai virus expressing Oct3/4, Sox2, c-Myc, and Klf4, which were subsequently induced into neural cells to build the cell model of AD. Using alkaline phosphatase staining, immunofluorescence staining, karyotype analysis, reverse transcription-polymerase chain reaction (RT-PCR), and teratoma formation in vitro, we demonstrated that the iPSC derived from PMBCs (PBMC-iPSC) had a normal karyotype and potential to differentiate into three embryonic layers. Immunofluorescence staining and quantitative real-time polymerase chain reaction (qPCR) suggested that PBMC-iPSCs were successfully differentiated into neural cells. Detection of beta-amyloid protein oligomer (AβO), beta-amyloid protein 1-40 (Aβ 1-40), and beta-amyloid protein 1-42 (Aβ 1-42) indicated that the AD cell model was satisfactorily constructed in vitro. In conclusion, this study has successfully generated an AD cell model with pathological features of beta-amyloid peptide deposition using PBMC from a patient with sAD.

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26

Castano, E. M., F. Prelli, T. Wisniewski, A. Golabek, R. A. Kumar, C. Soto, and B. Frangione. "Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E." Biochemical Journal 306, no. 2 (March 1, 1995): 599–604. http://dx.doi.org/10.1042/bj3060599.

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A central event in Alzheimer's disease is the conformational change from normally circulating soluble amyloid beta peptides (A beta) and tau proteins into amyloid fibrils, in the form of senile plaques and neurofibrillary tangles respectively. The apolipoprotein E (apoE) gene locus has recently been associated with late-onset Alzheimer's disease. It is not know whether apoE plays a direct role in the pathogenesis of the disease. In the present work we have investigated whether apoE can affect the known spontaneous in vitro formation of amyloid-like fibrils by synthetic A beta analogues using a thioflavine-T assay for fibril formation, electron microscopy and Congo Red staining. Our results show that, under the conditions used, apoE directly promotes amyloid fibril formation, increasing both the rate of fibrillogenesis and the total amount of amyloid formed. ApoE accelerated fibril formation of both wild-type A beta-(1-40) and A beta-(1-40A), an analogue created by the replacement of valine with alanine at residue 18, which alone produces few amyloid-like fibrils. However, apoE produced only a minimal effect on A beta-(1-40Q), found in the Dutch variant of Alzheimer's disease. When recombinant apoE isoforms were used, apoE4 was more efficient than apoE3 at enhancing amyloid formation. These in vitro observations support the hypothesis that apoE acts as a pathological chaperone, promoting the beta-pleated-sheet conformation of soluble A beta into amyloid fibres, and provide a possible explanation for the association of the apoE4 genetic isoform with Alzheimer's disease.

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27

Pannee, Josef, Johan Gobom, Madalina Opperman, Alan Atkins, Henrik Zetterberg, Lennart Minthon, Kaj Blennow, Oskar Hansson, and Erik Portelius. "O2-03-06: An LC-MS/MS-based method for quantification of beta-amyloid-1-38, beta-amyloid-1-40 and beta-amyloid-1-42 in the cerebrospinal fluid of Alzheimer's patients and healthy controls." Alzheimer's & Dementia 8, no. 4S_Part_7 (July 2012): P240—P241. http://dx.doi.org/10.1016/j.jalz.2012.05.639.

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28

Unlap, Menjor, Corey Williams, Darryl Morin, Brian Siroky, Attila Fintha, Amanda Fuson, Layla Dodgen, et al. "Amyloid Beta Peptide 1-40 Stimulates the Na+ / Ca2+ Exchange Activity of SNCX." Current Neurovascular Research 2, no. 1 (January 1, 2005): 3–12. http://dx.doi.org/10.2174/1567202052773472.

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29

Gao, Qi, Yuqiang Fang, Shiqing Zhang, Hung-Wing Li, Ken K. L. Yung, and King Wai Chiu Lai. "Biophysical Characteristics of Human Neuroblastoma Cell in Oligomeric $\beta $ -Amyloid (1–40) Cytotoxicity." IEEE Transactions on NanoBioscience 17, no. 1 (January 2018): 70–77. http://dx.doi.org/10.1109/tnb.2018.2800723.

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30

Stamatelopoulos, Kimon, and Konstantinos Stellos. "Circulating Amyloid-Beta (1-40) Predicts Clinical Outcomes in Patients With Heart Failure." Revista Española de Cardiología (English Edition) 70, no. 11 (November 2017): 905–6. http://dx.doi.org/10.1016/j.rec.2017.05.026.

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31

Vivekanandan, Subramanian, Jeffrey R. Brender, Shirley Y. Lee, and Ayyalusamy Ramamoorthy. "A partially folded structure of amyloid-beta(1–40) in an aqueous environment." Biochemical and Biophysical Research Communications 411, no. 2 (July 2011): 312–16. http://dx.doi.org/10.1016/j.bbrc.2011.06.133.

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32

Shi, Xiang, Xiaoguang Lu, Libin Zhan, Li Liu, MingZhong Sun, Xiaoyang Gong, Hua Sui, et al. "Rat hippocampal proteomic alterations following intrahippocampal injection of amyloid beta peptide (1–40)." Neuroscience Letters 500, no. 2 (August 2011): 87–91. http://dx.doi.org/10.1016/j.neulet.2011.06.009.

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33

Brining, Sheryl K., Nong Chen, Daniel Yi, and Andreas Chrambach. "Gel electrophoretic distinction between toxic and nontoxic forms of beta-amyloid (1—40)." Electrophoresis 20, no. 7 (June 1, 1999): 1398–402. http://dx.doi.org/10.1002/(sici)1522-2683(19990601)20:7<1398::aid-elps1398>3.0.co;2-1.

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34

Wiltfang, Jens, Alexandr Smirnov, Beate Schnierstein, Georg Kelemen, Uta Matthies, Hans-Wolfgang Klafki, Matthias Staufenbiel, Gerald Hüther, Eckhardt Rüther, and Johannes Kornhuber. "Improved electrophoretic separation and immunoblotting of beta-amyloid (Aβ) peptides 1-40, 1-42, and 1-43." Electrophoresis 18, no. 3-4 (1997): 527–32. http://dx.doi.org/10.1002/elps.1150180332.

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35

Ntarakas, Nikolaos, Inna Ermilova, and Alexander P. Lyubartsev. "Effect of lipid saturation on amyloid-beta peptide partitioning and aggregation in neuronal membranes: molecular dynamics simulations." European Biophysics Journal 48, no. 8 (October 26, 2019): 813–24. http://dx.doi.org/10.1007/s00249-019-01407-x.

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Abstract Aggregation of amyloid-$$\beta $$β (Aβ) peptides, cleaved from the amyloid precursor protein, is known as a precursor of the Alzheimer’s disease (AD). It is also known that Alzheimer’s disease is characterized by a substantial decrease of the amount of polyunsaturated lipids in the neuronal membranes of the frontal gray matter. To get insight into possible interconnection of these phenomena, we have carried out molecular dynamics simulations of two fragments of A$$\beta $$β peptide, A$$\beta $$β$$_{1-28}$$1-28 and A$$\beta $$β$$_{26-40}$$26-40, in four different lipid bilayers: two monocomponent ones (14:0-14:0 PC, 18:0-22:6 PC), and two bilayers containing mixtures of 18:0-18:0 PE, 22:6-22:6 PE, 16:0-16:0 PC and 18:1-18:1 PC lipids of composition mimicking neuronal membranes in a “healthy” and “AD” brain. The simulations showed that the presence of lipids with highly unsaturated 22:6cis fatty acids chains strongly affects the interaction of amyloid-$$\beta $$β peptides with lipid membranes. The polyunsaturated lipids cause stronger adsorption of A$$\beta $$β-peptides by the membrane and lead to weaker binding between peptides when the latter form aggregates. This difference in the behaviour observed in monocomponent bilayers is propagated in a similar fashion to the mixed membranes mimicking composition of neuronal membranes in “healthy” and “AD” brains, with “healthy” membrane having higher fraction of polyunsaturated lipids. Our simulations give strong indication that it can be physical–chemical background of the interconnection between amyloid fibrillization causing Alzheimer’s disease, and content of polyunsaturated lipids in the neuronal membranes.

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36

Bjerke, Maria, Charisse Somers, Naomi De Roeck, Anne Sieben, Ellis Niemantsverdriet, Yannick Vermeiren, Hanne Struyfs, et al. "P1-237: IMPROVED DIAGNOSTIC ACCURACY USING THE CEREBROSPINAL FLUID AMYLOID BETA 1-42/1-40 RATIO." Alzheimer's & Dementia 15 (July 2019): P327—P328. http://dx.doi.org/10.1016/j.jalz.2019.06.792.

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37

Brzyska, Maria, Katarzyna Trzesniewska, Tomasz Gers, and Danek Elbaum. "Discrete conformational changes as regulators of the hydrolytic properties of beta-amyloid (1-40)." FEBS Journal 273, no. 24 (November 15, 2006): 5598–611. http://dx.doi.org/10.1111/j.1742-4658.2006.05549.x.

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38

Mohanty, Joy G., Luke B. Ravi, Francis J. Chrest, Enika Nagababu, Viswanathan Natarajan, and Joseph M. Rifkind. "P2-134 Amyloid beta[1–40] fibrils mediate interactions between erythrocytes and endothelial cells." Neurobiology of Aging 25 (July 2004): S263. http://dx.doi.org/10.1016/s0197-4580(04)80881-9.

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39

Peng, Hao Benson, Keumhan Noh, Rui Sophie Pan, Victor Saldiva, Sylvia Serson, Anja Toscan, Ines deLannoy, and K. Sandy Pang. "Human amyloid-beta 1-40 disposition after intravenous and intracerebral injections in the rat." Drug Metabolism and Pharmacokinetics 34, no. 1 (January 2019): S65. http://dx.doi.org/10.1016/j.dmpk.2018.09.224.

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40

Nagaveni, V., V. V. S. Lakshmi, and S. Prabhakar. "Sulforaphane interaction with amyloid beta 1-40 peptide studied by electrospray ionization mass spectrometry." Rapid Communications in Mass Spectrometry 28, no. 20 (September 1, 2014): 2171–80. http://dx.doi.org/10.1002/rcm.7007.

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41

Banach, Mateusz, Leszek Konieczny, and Irena Roterman. "The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins." Molecules 24, no. 23 (December 3, 2019): 4395. http://dx.doi.org/10.3390/molecules24234395.

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Selected amyloid structures available in the Protein Data Bank have been subjected to a comparative analysis. Classification is based on the distribution of hydrophobicity in amyloids that differ with respect to sequence, chain length, the distribution of beta folds, protofibril structure, and the arrangement of protofibrils in each superfibril. The study set includes the following amyloids: Aβ (1–42), which is listed as Aβ (15–40) and carries the D23N mutation, and Aβ (11–42) and Aβ (1–40), both of which carry the E22Δ mutation, tau amyloid, and α-synuclein. Based on the fuzzy oil drop model (FOD), we determined that, despite their conformational diversity, all presented amyloids adopt a similar structural pattern that can be described as a ribbon-like micelle. The same model, when applied to globular proteins, results in structures referred to as “globular micelles,” emerging as a result of interactions between the proteins’ constituent residues and the aqueous solvent. Due to their composition, amyloids are unable to attain entropically favorable globular forms and instead attempt to limit contact between hydrophobic residues and water by producing elongated structures. Such structures typically contain quasi hydrophobic cores that stretch along the fibril’s long axis. Similar properties are commonly found in ribbon-like micelles, with alternating bands of high and low hydrophobicity emerging as the fibrils increase in length. Thus, while globular proteins are generally consistent with a 3D Gaussian distribution of hydrophobicity, the distribution instead conforms to a 2D Gaussian distribution in amyloid fibrils.

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Festa, Giulia, Francesco Mallamace, Giulia Maria Sancesario, Carmelo Corsaro, Domenico Mallamace, Enza Fazio, Laura Arcidiacono, et al. "Aggregation States of Aβ1–40, Aβ1–42 and Aβp3–42 Amyloid Beta Peptides: A SANS Study." International Journal of Molecular Sciences 20, no. 17 (August 24, 2019): 4126. http://dx.doi.org/10.3390/ijms20174126.

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Aggregation states of amyloid beta peptides for amyloid beta A β 1 – 40 to A β 1 – 42 and A β p 3 – 42 are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer’s disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A β p 3 – 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.

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43

Arispe, N., H. B. Pollard, and E. Rojas. "Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes." Proceedings of the National Academy of Sciences 90, no. 22 (November 15, 1993): 10573–77. http://dx.doi.org/10.1073/pnas.90.22.10573.

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44

Nishino, Satoshi, and Yuzo Nishida. "Oxygenation of amyloid beta-peptide (1–40) by copper(II) complex and hydrogen peroxide system." Inorganic Chemistry Communications 4, no. 2 (February 2001): 86–89. http://dx.doi.org/10.1016/s1387-7003(00)00213-6.

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45

Xiao, Lehui, Dan Zhao, Wing-Hong Chan, Martin M. F. Choi, and Hung-Wing Li. "Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots." Biomaterials 31, no. 1 (January 2010): 91–98. http://dx.doi.org/10.1016/j.biomaterials.2009.09.014.

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46

Chan, Ho-Man, Lehui Xiao, Kai-Ming Yeung, See-Lok Ho, Dan Zhao, Wing-Hong Chan, and Hung-Wing Li. "Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1–40) fibrillogenesis." Biomaterials 33, no. 18 (June 2012): 4443–50. http://dx.doi.org/10.1016/j.biomaterials.2012.03.024.

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47

Kowall, N. W., A. C. McKee, B. A. Yankner, and M. F. Beal. "In vivo neurotoxicity of beta-amyloid [β(1–40)] and the β(25–35) fragment." Neurobiology of Aging 13, no. 5 (September 1992): 537–42. http://dx.doi.org/10.1016/0197-4580(92)90053-z.

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48

Kucheryavykh, Lilia Y., Jescelica Ortiz-Rivera, Yuriy V. Kucheryavykh, Astrid Zayas-Santiago, Amanda Diaz-Garcia, and Mikhail Y. Inyushin. "Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors." International Journal of Molecular Sciences 20, no. 10 (May 20, 2019): 2482. http://dx.doi.org/10.3390/ijms20102482.

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Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies.

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Tamaoka, A., A. Odaka, Y. Ishibashi, M. Usami, N. Sahara, N. Suzuki, N. Nukina, H. Mizusawa, S. Shoji, and I. Kanazawa. "APP717 missense mutation affects the ratio of amyloid beta protein species (A beta 1-42/43 and a beta 1-40) in familial Alzheimer's disease brain." Journal of Biological Chemistry 269, no. 52 (December 1994): 32721–24. http://dx.doi.org/10.1016/s0021-9258(20)30050-8.

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50

Nomura, Izumi, Hajime Takechi, and Nobuo Kato. "Intraneuronally injected amyloid beta inhibits long-term potentiation in rat hippocampal slices." Journal of Neurophysiology 107, no. 9 (May 1, 2012): 2526–31. http://dx.doi.org/10.1152/jn.00589.2011.

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Extracellular accumulation of amyloid beta (Aβ) is a hallmark of Alzheimer's disease (AD). It has been reported that extracellular perfusion of Aβ inhibits long-term potentiation (LTP), which is strongly related to memory in animal models. However, it has recently been proposed that intracellular Aβ may be the first pathological change to occur in AD. Here, we have investigated the effect on LTP of intracellular injection of Aβ (Aβ1–40, Aβ1–42) into hippocampal pyramidal cells using patch-clamp technique. We found that injection of 1 nM Aβ1–42 completely blocked LTP, and extracellular perfusion of a p38 MAPK inhibitor or a metabotropic glutamate receptor blocker reversed these blocking effects on LTP. Furthermore, we have examined the effects of different concentrations of Aβ1–40 and Aβ1–42 on LTP and showed that Aβ1–40 required a 1,000-fold higher concentration to attenuate LTP than 1 nM Aβ1–42. These results indicate that LTP is impaired by Aβ injected into genetically wild-type neurons in the sliced hippocampus, suggesting an acute action of intracellular Aβ on the intracellular LTP-inducing machinery.

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